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Search results 601 to 686 out of 686 for Muc1

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Type Details Score
Strain
Attribute String: congenic, mutant strain, targeted mutation, transgenic
Publication
First Author: Wang P
Year: 2016
Journal: Int J Cancer
Title: Predictive imaging of chemotherapeutic response in a transgenic mouse model of pancreatic cancer.
Volume: 139
Issue: 3
Pages: 712-8
Strain
Attribute String: targeted mutation, transgenic, congenic
Genotype
Symbol: Tg(Ela1-TAg*)79Mjt/? Tg(MUC1)79.24Gend/?
Background: involves: C57BL/6 * DBA/2
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Kras/Kras<+> Ptf1a/Ptf1a<+> Tg(MUC1)79.24Gend/?
Background: B6.Cg-Kras Ptf1a Tg(MUC1)79.24Gend
Zygosity: cn
Has Mutant Allele: true
Genotype
Symbol: Il10/Il10 Tg(MUC1)79.24Gend/?
Background: B6.Cg-Il10 Tg(MUC1)79.24Gend
Zygosity: cx
Has Mutant Allele: true
Publication
First Author: Bornstein P
Year: 1993
Journal: Genomics
Title: Isolation and characterization of the mouse thrombospondin 3 (Thbs3) gene.
Volume: 15
Issue: 3
Pages: 607-13
Publication
First Author: Nakajima K
Year: 2020
Journal: Transl Psychiatry
Title: Ntrk1 mutation co-segregating with bipolar disorder and inherited kidney disease in a multiplex family causes defects in neuronal growth and depression-like behavior in mice.
Volume: 10
Issue: 1
Pages: 407
Publication
First Author: Siveke JT
Year: 2007
Journal: Cancer Cell
Title: Concomitant pancreatic activation of Kras(G12D) and Tgfa results in cystic papillary neoplasms reminiscent of human IPMN.
Volume: 12
Issue: 3
Pages: 266-79
Publication
First Author: Dvela-Levitt M
Year: 2019
Journal: Cell
Title: Small Molecule Targets TMED9 and Promotes Lysosomal Degradation to Reverse Proteinopathy.
Volume: 178
Issue: 3
Pages: 521-535.e23
Protein Domain
Type: Domain
Description: The SEA domain has been named after the first three proteins in which it was identified (Sperm protein, Enterokinase and Agrin). The SEA domain has around 120 residues, it is an extracellular domain found in a number of cell surface and secreted proteins in which it could be present in one or two copies []. Many SEA domains possess autoproteolysis activity. The SEA domain is closely associated with regions receiving extensive O-glycosylation and is present adjacent to the transmembrane segment in quite a number of type I transmembrane proteins on the cell surface, such as mucin-1 (MUC1) and Notch receptors and in type II single-pass transmembrane proteins such as enterokinase and matriptases. It also present in interphotoreceptor matrix proteoglycans (IMPG1 and IMPG2) []. It has been proposed that carbohydrates are required to stabilise SEA domains and protect them against proteolytic degradation and that the extent of substitution may control proteolytic processing [, ].The SEA domain contains an about 80-residue conserved region and an about 40-residue segment that separates the conserved region from the subsequent C-terminal domains with an alternating conformation of β-sheets and α-helices. Structural analysis of MUC1 SEA domain revealed that it adopts a ferredoxin-like fold in which the cleavage site is located in the middle of the β-hairpin of the second and third β-strands. MUC1 SEA domain undergoes autoproteolysis at the glycine-serine peptide bond and the Ser responsible of this activity is located in the consensus motif GSXXX (X: a hydrophobic residue) [, , ].Some proteins known to contain a SEA domain include:Vertebrate agrin, an heparan sulfate proteoglycan of the basal lamina of the neuromuscular junction. It is responsible for the clustering of acetylcholine receptors (AChRs) and other proteins at the neuromuscular junction.Mammalian enterokinase. It catalyses the conversion of trypsinogen to trypsin which in turn activates other proenzymes, including chymotrypsinogen, procarboxypeptidases, and proelastases.63kDa sea urchin sperm protein (SP63). It might mediate sperm-egg or sperm-matrix interactions.Animal perlecan, a heparan sulfate containing proteoglycan found in all basement membranes. It interacts with other basement membrane components such as laminin and collagen type IV and serves as an attachment substrate for cells.Some vertebrate epithelial mucins. They form a family of secreted and cell surface glycoproteins expressed by epithelial tissues and implicated in epithelial cell protection, adhesion modulation and signaling.Mammalian cell surface antigen 114/A10, an integral transmembrane protein that is highly expressed in hematopoietic progenitor cells and IL-3-dependent cell lines.
Protein Domain
Type: Homologous_superfamily
Description: The SEA domain has been named after the first three proteins in which it was identified (Sperm protein, Enterokinase and Agrin). The SEA domain has around 120 residues, it is an extracellular domain found in a number of cell surface and secreted proteins in which it could be present in one or two copies []. Many SEA domains possess autoproteolysis activity. The SEA domain is closely associated with regions receiving extensive O-glycosylation and is present adjacent to the transmembrane segment in quite a number of type I transmembrane proteins on the cell surface, such as mucin-1 (MUC1) and Notch receptors and in type II single-pass transmembrane proteins such as enterokinase and matriptases. It also present in interphotoreceptor matrix proteoglycans (IMPG1 and IMPG2) []. It has been proposed that carbohydrates are required to stabilise SEA domains and protect them against proteolytic degradation and that the extent of substitution may control proteolytic processing [, ].The SEA domain contains an about 80-residue conserved region and an about 40-residue segment that separates the conserved region from the subsequent C-terminal domains with an alternating conformation of β-sheets and α-helices. Structural analysis of MUC1 SEA domain revealed that it adopts a ferredoxin-like fold in which the cleavage site is located in the middle of the β-hairpin of the second and third β-strands. MUC1 SEA domain undergoes autoproteolysis at the glycine-serine peptide bond and the Ser responsible of this activity is located in the consensus motif GSXXX (X: a hydrophobic residue) [, , ].Some proteins known to contain a SEA domain include:Vertebrate agrin, an heparan sulfate proteoglycan of the basal lamina of the neuromuscular junction. It is responsible for the clustering of acetylcholine receptors (AChRs) and other proteins at the neuromuscular junction.Mammalian enterokinase. It catalyses the conversion of trypsinogen to trypsin which in turn activates other proenzymes, including chymotrypsinogen, procarboxypeptidases, and proelastases.63kDa sea urchin sperm protein (SP63). It might mediate sperm-egg or sperm-matrix interactions.Animal perlecan, a heparan sulfate containing proteoglycan found in all basement membranes. It interacts with other basement membrane components such as laminin and collagen type IV and serves as an attachment substrate for cells.Some vertebrate epithelial mucins. They form a family of secreted and cell surface glycoproteins expressed by epithelial tissues and implicated in epithelial cell protection, adhesion modulation and signaling.Mammalian cell surface antigen 114/A10, an integral transmembrane protein that is highly expressed in hematopoietic progenitor cells and IL-3-dependent cell lines.
Protein
Organism: Mus musculus/domesticus
Length: 630  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 798  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 8478  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 631  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2566  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 4499  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 631  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 336  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: false
Publication
First Author: Bork P
Year: 1995
Journal: Protein Sci
Title: The SEA module: a new extracellular domain associated with O-glycosylation.
Volume: 4
Issue: 7
Pages: 1421-5
Publication
First Author: Sasaki T
Year: 1998
Journal: FEBS Lett
Title: Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding activity.
Volume: 435
Issue: 2-3
Pages: 169-72
Publication
First Author: Costell M
Year: 1997
Journal: Eur J Biochem
Title: Characterization of recombinant perlecan domain I and its substitution by glycosaminoglycans and oligosaccharides.
Volume: 243
Issue: 1-2
Pages: 115-21
Publication
First Author: Pei J
Year: 2017
Journal: Protein Sci
Title: Expansion of divergent SEA domains in cell surface proteins and nucleoporin 54.
Volume: 26
Issue: 3
Pages: 617-630
Publication
First Author: Julien S
Year: 2009
Journal: Br J Cancer
Title: Sialyl-Tn vaccine induces antibody-mediated tumour protection in a relevant murine model.
Volume: 100
Issue: 11
Pages: 1746-54
Publication
First Author: Deguchi T
Year: 2010
Journal: Cancer Res
Title: Increased immunogenicity of tumor-associated antigen, mucin 1, engineered to express alpha-gal epitopes: a novel approach to immunotherapy in pancreatic cancer.
Volume: 70
Issue: 13
Pages: 5259-69
Publication
First Author: Apostolopoulos V
Year: 2000
Journal: Eur J Immunol
Title: A role for IL-5 in the induction of cytotoxic T lymphocytes in vivo.
Volume: 30
Issue: 6
Pages: 1733-9
Publication
First Author: Ilkovitch D
Year: 2009
Journal: Blood
Title: Urokinase-mediated recruitment of myeloid-derived suppressor cells and their suppressive mechanisms are blocked by MUC1/sec.
Volume: 113
Issue: 19
Pages: 4729-39
Publication
First Author: Madsen CB
Year: 2012
Journal: PLoS One
Title: Cancer associated aberrant protein O-glycosylation can modify antigen processing and immune response.
Volume: 7
Issue: 11
Pages: e50139
Publication
First Author: Kumar S
Year: 2015
Journal: Oncogene
Title: NCOA3-mediated upregulation of mucin expression via transcriptional and post-translational changes during the development of pancreatic cancer.
Volume: 34
Issue: 37
Pages: 4879-89
Publication
First Author: Farkas AM
Year: 2013
Journal: J Immunol
Title: Antigen choice determines vaccine-induced generation of immunogenic versus tolerogenic dendritic cells that are marked by differential expression of pancreatic enzymes.
Volume: 190
Issue: 7
Pages: 3319-27
Publication
First Author: Cantero-Recasens G
Year: 2022
Journal: Proc Natl Acad Sci U S A
Title: The ulcerative colitis-associated gene FUT8 regulates the quantity and quality of secreted mucins.
Volume: 119
Issue: 43
Pages: e2205277119
Publication  
First Author: Shalom-Barak T
Year: 2018
Journal: Mol Cell Biol
Title: Ligand-Dependent Corepressor (LCoR) Is a Rexinoid-Inhibited Peroxisome Proliferator-Activated Receptor γ-Retinoid X Receptor α Coactivator.
Volume: 38
Issue: 9
Publication
First Author: Rye PD
Year: 1996
Journal: Int J Cancer
Title: Brain metastasis model in athymic nude mice using a novel MUC1-secreting human breast-cancer cell line, MA11.
Volume: 68
Issue: 5
Pages: 682-7
Publication
First Author: Morikane K
Year: 1999
Journal: Cancer Immunol Immunother
Title: Organ-specific pancreatic tumor growth properties and tumor immunity.
Volume: 47
Issue: 5
Pages: 287-96
Publication
First Author: Argüeso P
Year: 2009
Journal: J Biol Chem
Title: Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier.
Volume: 284
Issue: 34
Pages: 23037-45
Publication  
First Author: Li W
Year: 2020
Journal: JCI Insight
Title: MUC1-C drives stemness in progression of colitis to colorectal cancer.
Volume: 5
Issue: 12
Publication  
First Author: Breugelmans T
Year: 2023
Journal: Cells
Title: IL-22-Activated MUC13 Impacts on Colonic Barrier Function through JAK1/STAT3, SNAI1/ZEB1 and ROCK2/MAPK Signaling.
Volume: 12
Issue: 9
Protein
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1243  
Fragment?: false
Publication
First Author: Kretschmer C
Year: 2011
Journal: Mol Cancer
Title: Identification of early molecular markers for breast cancer.
Volume: 10
Issue: 1
Pages: 15
Publication
First Author: Pietersz GA
Year: 1997
Journal: Cancer Immunol Immunother
Title: Comparison of the biological properties of two anti-mucin-1 antibodies prepared for imaging and therapy.
Volume: 44
Issue: 6
Pages: 323-8
Publication
First Author: Lofthouse SA
Year: 1997
Journal: Vaccine
Title: Induction of T1 (cytotoxic lymphocyte) and/or T2 (antibody) responses to a mucin-1 tumour antigen.
Volume: 15
Issue: 14
Pages: 1586-93
Publication
First Author: Nguyen TM
Year: 2019
Journal: PLoS One
Title: The proportion of alveolar type 1 cells decreases in murine hypoplastic congenital diaphragmatic hernia lungs.
Volume: 14
Issue: 4
Pages: e0214793
Publication
First Author: Saxena A
Year: 2013
Journal: Int J Colorectal Dis
Title: Mucus and adiponectin deficiency: role in chronic inflammation-induced colon cancer.
Volume: 28
Issue: 9
Pages: 1267-79
Protein
Organism: Mus musculus/domesticus
Length: 1151  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 573  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 573  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1950  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 439  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 423  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1194  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1927  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 908  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 811  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1099  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2034  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 799  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 620  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1099  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1319  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 855  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 829  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 855  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1069  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1054  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 3707  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2672  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4375  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4383  
Fragment?: false